Protein-O-mannosyltransferases in virulence and development
Protein-O-mannosyltransferases (Pmt proteins) catalyse the addition of mannose to serine or threonine residues of secretory proteins. This modification was described first for yeast and later for other fungi, mammals, insects and recently also for bacteria. O-mannosylation depends on specific isofor...
Saved in:
Published in | Cellular and molecular life sciences : CMLS Vol. 65; no. 4; pp. 528 - 544 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Basel
Basel : SP Birkhäuser Verlag Basel
01.02.2008
Birkhäuser-Verlag Springer Nature B.V |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Protein-O-mannosyltransferases (Pmt proteins) catalyse the addition of mannose to serine or threonine residues of secretory proteins. This modification was described first for yeast and later for other fungi, mammals, insects and recently also for bacteria. O-mannosylation depends on specific isoforms of the three Pmt1, 2 and 4 subfamilies. In fungi, O-mannosylation determines the structure and integrity of cell walls, as well as cellular differentiation and virulence. O-mannosylation of specific secretory proteins of the human fungal pathogen Candida albicans and of the bacterial pathogen Mycobacterium tuberculosis contributes significantly to virulence. In mammals and insects, Pmt proteins are essential for cellular differentiation and development, while lack of Pmt activity causes Walker-Warburg syndrome (muscular dystrophy) in humans. The susceptibility of human cells to certain viruses may also depend on O-mannosyl chains. This review focuses on the various roles of Pmt proteins in cellular differentiation, development and virulence. |
---|---|
Bibliography: | http://dx.doi.org/10.1007/s00018-007-7409-z ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 1420-682X 1420-9071 |
DOI: | 10.1007/s00018-007-7409-z |